1uvu

BOVINE THROMBIN--BM12.1700 COMPLEX

Method: X-RAY DIFFRACTION Dmax: 57.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

THROMBIN

OrganismNot specified

UniProt P00735

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 367–625 Chain L; UniProt 318–366 Not recorded DCH 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

30 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THRB_BOVIN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain L; PDBConstruct 1–49; UniProt 318–366 Author chain H; PDBConstruct 1–259; UniProt 367–625

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1uvu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1uvu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1uvu
Deposition date deposition_date1996-10-16
Structure title titleBOVINE THROMBIN--BM12.1700 COMPLEX
Keywords keywordsSERINE PROTEASE, HYDROLASE, THROMBIN, BLOOD COAGULATION; SERINE PROTEASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.62
Radius of gyration Rg (electron density) rg_electron17.49
Forward intensity I(0) i016411900.00
Molecular weight molecular_weight31217.0 kDa
Excluded volume excluded_volume39328 ų
Envelope volume envelope_volume44070 ų
Hydration-shell volume shell_volume20241 ų
Envelope diameter envelope_diameter57.7
Shell Rg shell_rg24.51
Envelope Rg envelope_rg17.83
Shape Rg shape_rg17.47
Total Rg total_rg18.54
Total atoms total_atoms2203
Residues n_residues235
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax57.2
Rg (real space) rg_real18.47
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.6410e+07
I(0) uncertainty (real space) i0_real_error1.9240e+05
Rg (reciprocal space) rg_reciprocal18.49
I(0) (reciprocal space) i0_reciprocal16410000.0000
Solution quality estimate total_estimate0.8960
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.465
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6039000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1uvu.1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id1uvuH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1uvuH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)